Evidence map›Paper›PMID 18794844›Full record

ArticleNature structural & molecular biology2008

Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator.

Ying Feng, Mo Chen, James L Manley

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

56 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Ying FengDepartment of Biological Sciences, Columbia University, 1212 Amsterdam Avenue, New York, New York 10027, USA.
Mo Chen
James L Manley

Funding

MECHANISMS OF ALTERNATIVE SPLICING OF PRE MRNAR01GM048259 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1992 to 2015
$5.2M
MECHANISMS OF ALTERNATIVE SPLICING OF PRE MRNAR37GM048259 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 1996 to 2005
$2.8M
NIGMS NIH HHS GM48259NIGMS NIH HHS R01 GM048259NIGMS NIH HHS R37 GM048259
6 · The paper itself

Abstract

SRp38 is an atypical SR protein that functions as a general splicing repressor when dephosphorylated. We now show that phosphorylated SRp38 functions as a sequence-specific splicing activator. Unlike characterized splicing activators, SRp38 functions in the absence of other SR proteins but requires a cofactor for activity. SRp38 was able to induce formation of splicing complex A in the absence of the cofactor, but this factor was necessary for progression to complexes B and C. Mechanistically, SRp38 strengthens the ability of the U1 and U2 small nuclear ribonucleoproteins to stably recognize the pre-mRNA. Extending these findings, analysis of alternative splicing of pre-mRNA encoding the glutamate receptor B revealed that SRp38 alters its splicing pattern in a sequence-specific manner. Together, our data demonstrate that SRp38, in addition to its role as a splicing repressor, can function as an unusual sequence-specific splicing activator.

Indexed as

AnimalsBase SequenceBinding SitesCell Cycle ProteinsCell LineChickensExonsNeoplasm ProteinsPhosphorylationProtein BindingRepressor ProteinsRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA SplicingCell Cycle ProteinsNeoplasm ProteinsRepressor ProteinsRibonucleoprotein, U1 Small NuclearRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID18794844
PMCPMC2668916

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.